› 1slh

X-ray diffraction
3Å resolution

Mycobacterium tuberculosis dUTPase complexed with magnesium and dUDP

Released:
DOI: 10.2210/pdb1slh/pdb
PDB entry 1slh coloured by chain, front view.
PDB entry 1slh coloured by chain, side view.
PDB entry 1slh coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism.
Chan S, Segelke B, Lekin T, Krupka H, Cho US, Kim MY, So M, Kim CY, Naranjo CM, Rogers YC, Park MS, Waldo GS, Pashkov I, Cascio D, Perry JL, Sawaya MR
J Mol Biol 341 503-17 (2004)
PMID: 15276840

Function and Biology Details

Reaction catalysed: 
dUTP + H(2)O = dUMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-161882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 174 amino acids
Theoretical weight: 17.99 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNS5 (Residues: 1-154; Coverage: 100%)
Gene names: MTCY05A6.18c, Rv2697c, dut
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

3 bound ligands:
Ligand MG 3 x MG
Ligand DUD 3 x DUD
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P3121
Unit cell:
a: 108.273Å b: 108.273Å c: 100.792Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.224 0.265
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The phage-related chromosomal islands of Gram-positive bacteria.
Novick et al. (2010)
5 more

4 mentions without citation

In Thermoanaerobacterium thermosulfurigenes EM1 S-layer homology domains do not attach to peptidoglycan.
Brechtel et al. (1999)
3 more